Post-translational modification of proteins by N-acetylglucosamine (O-GlcNAc) is carried out by a single glycosyltransferase, OGT. Two independent groups have generated structures of ternary complexes that elegantly illuminate substrate and product binding modes, and thus the overall reaction coordinate, but the respective authors differ in their choice of catalytic base.
Change history
13 November 2012
In the version of this article initially published online, the wrong article was listed as reference 4. The error has been corrected for the PDF and HTML versions of this article.
References
Yuzwa, S.A. et al. Nat. Chem. Biol. 8, 393–399 (2012).
Yi, W. et al. Science 337, 975–980 (2012).
Lazarus, M.B., Nam, Y., Jiang, J., Sliz, P. & Walker, S. Nature 469, 564–567 (2011).
Gloster, T.M. et al. Nat. Chem. Biol. 7, 174–181 (2011).10.1038/nchembio.520
Lazarus, M.B. et al. Nat. Chem. Biol. 8, 966–968 (2012).
Schimpl, M. et al. Nat. Chem. Biol. 8, 969–974 (2012).
Jancan, I. & Macnaughtan, M.A. Anal. Chim. Acta 749, 63–69 (2012).
Koivula, A. et al. J. Am. Chem. Soc. 124, 10015–10024 (2002).
Tvaroška, I., Kozmon, S., Wimmerova, M. & Koca, J. J. Am. Chem. Soc. 134, 15563–15571 (2012).
Author information
Authors and Affiliations
Corresponding authors
Ethics declarations
Competing interests
The authors declare no competing financial interests.
Rights and permissions
About this article
Cite this article
Withers, S., Davies, G. The case of the missing base. Nat Chem Biol 8, 952–953 (2012). https://doi.org/10.1038/nchembio.1117
Published:
Issue Date:
DOI: https://doi.org/10.1038/nchembio.1117
- Springer Nature America, Inc.
This article is cited by
-
Molecular basis for bacterial N-glycosylation by a soluble HMW1C-like N-glycosyltransferase
Nature Communications (2023)